HOPS drives vacuole fusion by binding the vacuolar SNARE complex and the Vam7 PX domain via two distinct sites

DC FieldValueLanguage
dc.contributor.authorKraemer, Lukas
dc.contributor.authorUngermann, Christian
dc.date.accessioned2021-12-23T16:05:16Z-
dc.date.available2021-12-23T16:05:16Z-
dc.date.issued2011
dc.identifier.issn10591524
dc.identifier.urihttps://osnascholar.ub.uni-osnabrueck.de/handle/unios/6888-
dc.description.abstractMembrane fusion within the endomembrane system follows a defined order of events: membrane tethering, mediated by Rabs and tethers, assembly of soluble N-ethylmaleimide-sensitive factor (NSF) attachment protein receptor (SNARE) complexes, and lipid bilayer mixing. Here we present evidence that the vacuolar HOPS tethering complex controls fusion through specific interactions with the vacuolar SNARE complex (consisting of Vam3, Vam7, Vti1, and Nyv1) and the N-terminal domains of Vam7 and Vam3. We show that homotypic fusion and protein sorting (HOPS) binds Vam7 via its subunits Vps16 and Vps18. In addition, we observed that Vps16, Vps18, and the Sec1/Munc18 protein Vps33, which is also part of the HOPS complex, bind to the Q-SNARE complex. In agreement with this observation, HOPS-stimulated fusion was inhibited if HOPS was preincubated with the minimal Q-SNARE complex. Importantly, artificial targeting of Vam7 without its PX domain to membranes rescued vacuole morphology in vivo, but resulted in a cytokinesis defect if the N-terminal domain of Vam3 was also removed. Our data thus support a model of HOPS-controlled membrane fusion by recognizing different elements of the SNARE complex.
dc.description.sponsorshipDeutsche Forschungsgemeinschaft (DFG)German Research Foundation (DFG) [UN111/4-2]; Sonderforschungsbereich (SFB)German Research Foundation (DFG) [431, 944]; Hans-Muhlenhoff Foundation; We thank Christine Boeddinghaus for the generation of some of the Vam7 truncation constructs and all coworkers for discussions throughout this study. This work has been supported by the Deutsche Forschungsgemeinschaft (DFG) (UN111/4-2), the Sonderforschungsbereich (SFB) 431 and 944, and the Hans-Muhlenhoff Foundation (to C. U.).
dc.language.isoen
dc.publisherAMER SOC CELL BIOLOGY
dc.relation.ispartofMOLECULAR BIOLOGY OF THE CELL
dc.subjectCell Biology
dc.subjectDOCKING
dc.subjectMECHANISM
dc.subjectMEMBRANE-FUSION
dc.subjectN-TERMINAL PEPTIDE
dc.subjectPROTEIN
dc.subjectPURIFICATION
dc.subjectRAB
dc.subjectREQUIRES
dc.subjectT-SNARE
dc.subjectYEAST VACUOLE
dc.titleHOPS drives vacuole fusion by binding the vacuolar SNARE complex and the Vam7 PX domain via two distinct sites
dc.typejournal article
dc.identifier.doi10.1091/mbc.E11-02-0104
dc.identifier.isiISI:000292687800016
dc.description.volume22
dc.description.issue14
dc.description.startpage2601
dc.description.endpage2611
dc.identifier.eissn19394586
dc.publisher.place8120 WOODMONT AVE, STE 750, BETHESDA, MD 20814-2755 USA
dcterms.isPartOf.abbreviationMol. Biol. Cell
dcterms.oaStatusGreen Published, hybrid, Green Submitted
crisitem.author.netidUnCh999-
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